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Backbone conformation of amino acids

✍ Scribed by V. Saisekharan; P. K. Ponnuswamy


Publisher
Wiley (John Wiley & Sons)
Year
1969
Tongue
English
Weight
206 KB
Volume
7
Category
Article
ISSN
0006-3525

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πŸ“œ SIMILAR VOLUMES


Backbone and side-chain conformations of
✍ V. Sasisekharan; P. K. Ponnuswamy πŸ“‚ Article πŸ“… 1970 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 198 KB πŸ‘ 2 views

Although the conformations of two linked peptide units both with glycyl and alanyl residues have been extensively studied,'-$ no systematic investigation of the energies of conformations of two linked peptide units with side chains beyond the CB atom and a comparison with the available crystallograp

Photomodulation of conformational states
✍ Christian Renner; Raymond Behrendt; Sebastian SpΓΆrlein; Josef Wachtveitl; Luis M πŸ“‚ Article πŸ“… 2000 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 528 KB

The thioredoxin reductase active-site fragment H-Ala-Cys-Ala-Thr-Cys-Asp-Gly-Phe-OH [134 -141], which is known for its high tendency to assume an almost identical conformation as in the intact enzyme, was backbone cyclized with the photoresponsive (4-amino)phenylazobenzoic acid (APB) to produce a mo

Residual Dipolar Couplings in Short Pept
✍ Markus B. Schmid; Matthias Fleischmann; Valerio D'Elia; Oliver Reiser; Wolfram G πŸ“‚ Article πŸ“… 2009 πŸ› John Wiley and Sons 🌐 English βš– 520 KB

## Abstract **A flexible tool for rigid systems**. Residual dipolar couplings (RDCs) have proven to be valuable NMR structural parameters that provide insights into the backbone conformations of short linear peptidic foldamers, as illustrated here. This study demonstrates that RDCs at natural abund